ID A0A060NIP9_9BURK Unreviewed; 741 AA.
AC A0A060NIP9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
GN Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN ORFNames=SRAA_2147 {ECO:0000313|EMBL:BAO82001.1};
OS Serpentinimonas raichei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO82001.1, ECO:0000313|Proteomes:UP000067461};
RN [1] {ECO:0000313|EMBL:BAO82001.1, ECO:0000313|Proteomes:UP000067461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:BAO82001.1,
RC ECO:0000313|Proteomes:UP000067461};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-
CC CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-
CC Rule:MF_00641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001699, ECO:0000256|HAMAP-
CC Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00641};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC ECO:0000256|RuleBase:RU003572}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC ECO:0000256|RuleBase:RU003572}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
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DR EMBL; AP014568; BAO82001.1; -; Genomic_DNA.
DR RefSeq; WP_045532671.1; NZ_AP014568.1.
DR AlphaFoldDB; A0A060NIP9; -.
DR STRING; 1458425.SRAA_2147; -.
DR KEGG; cbaa:SRAA_2147; -.
DR HOGENOM; CLU_028446_1_0_4; -.
DR OrthoDB; 9762054at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000067461; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.360; Malate synthase, domain 3; 2.
DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
DR HAMAP; MF_00641; Malate_synth_G; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR001465; Malate_synthase_TIM.
DR InterPro; IPR006253; Malate_synthG.
DR InterPro; IPR048355; MS_C.
DR InterPro; IPR048356; MS_N.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR InterPro; IPR048357; MSG_insertion.
DR NCBIfam; TIGR01345; malate_syn_G; 1.
DR PANTHER; PTHR42739; MALATE SYNTHASE G; 1.
DR PANTHER; PTHR42739:SF1; MALATE SYNTHASE G; 1.
DR Pfam; PF20659; MS_C; 1.
DR Pfam; PF20656; MS_N; 1.
DR Pfam; PF01274; MS_TIM-barrel; 1.
DR Pfam; PF20658; MSG_insertion; 1.
DR SUPFAM; SSF51645; Malate synthase G; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641};
KW Reference proteome {ECO:0000313|Proteomes:UP000067461};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00641}.
FT DOMAIN 17..78
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 161..236
FT /note="Malate synthase G alpha-beta insertion"
FT /evidence="ECO:0000259|Pfam:PF20658"
FT DOMAIN 338..590
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 608..716
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 647
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT BINDING 119
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 126..127
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 277
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 314
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 341
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 443
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 468..471
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 552
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT MOD_RES 633
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
SQ SEQUENCE 741 AA; 80035 MW; 01A941CA85A519E3 CRC64;
MSTARTAAGR LQVASALYDF VNHEVLPGTG IESAPFWAGF EALVTDLAPK NAALLAERDR
MQSELDRWHR AHPGPITDMP AYRQFLEGIG YLVPAPSGVR ASTANVDAEL ALQAGPQLVV
PILNARYALN AANARWGSLY DALYGTDAIP ESEGCERGRG YNPLRGARVI AFARQFLDQA
APLAIESHQD ACGYRIVAGA LQVSLDDGQQ TGLRQPQQLL GYRGAPEAPS ALLLQHHGMH
IEIVLDRQTA IGRTDPAGIS DVVLESALST ILDLEDSVAA VDAEDKILGY RNWLGILRGS
LTETFDKGGI SLTRGLNPDR RYTRPDGGEL RLHGRSLLFV RNVGHLMSNP AILYTDAAGV
AREIPEGILD AVLTTTIALH DLQGHGRLPS GEPVRNSRSG SVYIVKPKMH GPQEVAFAAE
LFGRVERLLG LPESTVKLGI MDEERRTSVN LKACIAAAAS RVAFINTGFL DRTGDEMHTA
MQAGPMVRKG EMKSSAWIAA YERNNVLVGL GMGLRGRAQI GKGMWAMPDL MAEMLKQKIA
HPKAGANTAW VPSPTAATLH ALHYHQVNVA EVQQELERID ADAERAALLQ GLLTVPVAAQ
PNWSEADKQA ELDNNIQGIL GYVVRWVDQG VGCSKVPDIN DIGLMEDRAT LRISSQHVAN
WLLHGVVSEA QVRQSFARMA AKVDAQNAAD PAYRSLLAHP DGAAYQAALD LVFKGCAQPS
GYTEPLLHAW RLKVKAQSAR A
//
